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PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
Authors:Badrick Alison C  Hamilton Amanda J  Bernhardt Paul V  Jones Christopher E  Kappler Ulrike  Jennings Michael P  McEwan Alastair G
Institution:Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Abstract:PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that induces photosynthesis gene expression in response to a decrease in oxygen tension. Although Sco proteins have been shown to bind copper the observation that they are structurally-related to thioredoxins suggested that they might possess thiol-disulfide oxidoreductase activity. Our results show that PrrC reduces Cu(2+) to Cu(+) and possesses disulfide reductase activity. These results indicate that some bacterial Sco proteins may have biochemical properties that are distinct from those of mitochondrial Sco proteins.
Keywords:BC  bathocuproine 2  9-dimethyl-4  7-diphenyl-1  10-phenanthroline  BSA  bovine serum albumin  Co(trans-diammac)  trans-6  13-dimethyl-(1  4  8  11-tetraazacyclotetradecane-6  13-diamine)cobalt(III) perchlorate  cPrrC  cleaved PrrC  DTNB  5  5-dithiobis(2-nitrobenzoic acid)  DTT  dithiothreitol  (2R  3R)-1  4-bis-sulfanylbutane-2  3-diol  EPR  Electron Paramagnetic Resonance  htPrrC  6×-his-tagged PrrC  IPTG  d-thiogalactopyranoside" target="_blank">isopropyl-β-d-thiogalactopyranoside  oxPrrC  oxidised PrrC  PrrC  photosynthetic regulatory response  rPrrC  reduced PrrC  Sco  synthesis of cytochrome oxidase  Trx  thioredoxin
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